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Conserved domains on  [gi|515869683|ref|NP_001265520|]
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lipoyl synthase, mitochondrial isoform 4 precursor [Homo sapiens]

Protein Classification

LIAS_N domain-containing protein( domain architecture ID 11245877)

LIAS_N domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LIAS_N pfam16881
N-terminal domain of lipoyl synthase of Radical_SAM family; LIAS_N is found as the N-terminal ...
 15-111 1.38e-67

N-terminal domain of lipoyl synthase of Radical_SAM family; LIAS_N is found as the N-terminal domain of the Radical_SAM family in the members that are lipoyl synthase enzymes, particularly the mitochondrial ones in metazoa but also those in bacteria.


:

Pssm-ID: 465296 [Multi-domain]  Cd Length: 97  Bit Score: 199.28  E-value: 1.38e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869683   15 RVFGRYFCSPVRPLSSLPDKKKELLQNGPDLQDFVSGDLADRSTWDEYKGNLKRQKGERLRLPPWLKTEIPMGKNYNKLK 94
Cdd:pfam16881   1 RVFGSHLCSPASTSSSLPDEKREFLQNGPDLQDFVSGDLSDKSTWAEYKGNLKRPKGERLRLPPWLKTKIPLGKNYNKIK 80

                          90
                  ....*....|....*..
gi 515869683   95 NTLRNLNLHTVCEEARC 111
Cdd:pfam16881  81 NTLRNLNLHTVCEEARC 97
 
Name Accession Description Interval E-value
LIAS_N pfam16881
N-terminal domain of lipoyl synthase of Radical_SAM family; LIAS_N is found as the N-terminal ...
 15-111 1.38e-67

N-terminal domain of lipoyl synthase of Radical_SAM family; LIAS_N is found as the N-terminal domain of the Radical_SAM family in the members that are lipoyl synthase enzymes, particularly the mitochondrial ones in metazoa but also those in bacteria.


Pssm-ID: 465296 [Multi-domain]  Cd Length: 97  Bit Score: 199.28  E-value: 1.38e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869683   15 RVFGRYFCSPVRPLSSLPDKKKELLQNGPDLQDFVSGDLADRSTWDEYKGNLKRQKGERLRLPPWLKTEIPMGKNYNKLK 94
Cdd:pfam16881   1 RVFGSHLCSPASTSSSLPDEKREFLQNGPDLQDFVSGDLSDKSTWAEYKGNLKRPKGERLRLPPWLKTKIPLGKNYNKIK 80

                          90
                  ....*....|....*..
gi 515869683   95 NTLRNLNLHTVCEEARC 111
Cdd:pfam16881  81 NTLRNLNLHTVCEEARC 97
PLN02428 PLN02428
lipoic acid synthase
 22-132 6.71e-32

lipoic acid synthase


Pssm-ID: 215236 [Multi-domain]  Cd Length: 349  Bit Score: 115.62  E-value: 6.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869683  22 CSPVRPLSSLPDKKKELLQNGPDLQDFVSGDladrsTWDEYKGNLKRQkgerLRLPPWLKTEIPMGKNYNKLKNTLRNLN 101
Cdd:PLN02428   6 TTAPQTPQTLAALRARLASESPSLGDFVSLG-----PYTLGSYGRDKP----LPKPKWLRQRAPGGEKYTEIKEKLRELK 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 515869683 102 LHTVCEEARCPNIGECWGGGEYATATATIMV 132
Cdd:PLN02428  77 LNTVCEEAQCPNIGECWNGGGTGTATATIMI 107
LipA COG0320
Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway ...
 67-133 1.37e-30

Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway/BioSystem: Lipoate biosynthesis


Pssm-ID: 440089 [Multi-domain]  Cd Length: 306  Bit Score: 111.35  E-value: 1.37e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515869683  67 KRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGeyataTATIMVG 133
Cdd:COG0320   13 RNPETPILRKPDWLRVKLPTGPEYAEVKKLLREHKLHTVCEEARCPNIGECWSRG-----TATFMIL 74
lipA TIGR00510
lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in ...
 65-132 5.84e-22

lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in yeast and Arabidopsis. It generates lipoic acid, a thiol antioxidant that is linked to a specific Lys as prosthetic group for the pyruvate and alpha-ketoglutarate dehydrogenase complexes and the glycine-cleavage system. The family shows strong sequence conservation. [Biosynthesis of cofactors, prosthetic groups, and carriers, Lipoate]


Pssm-ID: 273111  Cd Length: 302  Bit Score: 88.74  E-value: 5.84e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515869683   65 NLKRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGeyataTATIMV 132
Cdd:TIGR00510   6 NPIPNKEILLRKPEWLKIKLPLGTVIAQIKNTMKNKGLHTVCEEASCPNLTECWNHG-----TATFMI 68
 
Name Accession Description Interval E-value
LIAS_N pfam16881
N-terminal domain of lipoyl synthase of Radical_SAM family; LIAS_N is found as the N-terminal ...
 15-111 1.38e-67

N-terminal domain of lipoyl synthase of Radical_SAM family; LIAS_N is found as the N-terminal domain of the Radical_SAM family in the members that are lipoyl synthase enzymes, particularly the mitochondrial ones in metazoa but also those in bacteria.


Pssm-ID: 465296 [Multi-domain]  Cd Length: 97  Bit Score: 199.28  E-value: 1.38e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869683   15 RVFGRYFCSPVRPLSSLPDKKKELLQNGPDLQDFVSGDLADRSTWDEYKGNLKRQKGERLRLPPWLKTEIPMGKNYNKLK 94
Cdd:pfam16881   1 RVFGSHLCSPASTSSSLPDEKREFLQNGPDLQDFVSGDLSDKSTWAEYKGNLKRPKGERLRLPPWLKTKIPLGKNYNKIK 80

                          90
                  ....*....|....*..
gi 515869683   95 NTLRNLNLHTVCEEARC 111
Cdd:pfam16881  81 NTLRNLNLHTVCEEARC 97
PLN02428 PLN02428
lipoic acid synthase
 22-132 6.71e-32

lipoic acid synthase


Pssm-ID: 215236 [Multi-domain]  Cd Length: 349  Bit Score: 115.62  E-value: 6.71e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515869683  22 CSPVRPLSSLPDKKKELLQNGPDLQDFVSGDladrsTWDEYKGNLKRQkgerLRLPPWLKTEIPMGKNYNKLKNTLRNLN 101
Cdd:PLN02428   6 TTAPQTPQTLAALRARLASESPSLGDFVSLG-----PYTLGSYGRDKP----LPKPKWLRQRAPGGEKYTEIKEKLRELK 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 515869683 102 LHTVCEEARCPNIGECWGGGEYATATATIMV 132
Cdd:PLN02428  77 LNTVCEEAQCPNIGECWNGGGTGTATATIMI 107
LipA COG0320
Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway ...
 67-133 1.37e-30

Lipoate synthase [Coenzyme transport and metabolism]; Lipoate synthase is part of the Pathway/BioSystem: Lipoate biosynthesis


Pssm-ID: 440089 [Multi-domain]  Cd Length: 306  Bit Score: 111.35  E-value: 1.37e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515869683  67 KRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGeyataTATIMVG 133
Cdd:COG0320   13 RNPETPILRKPDWLRVKLPTGPEYAEVKKLLREHKLHTVCEEARCPNIGECWSRG-----TATFMIL 74
PRK05481 PRK05481
lipoyl synthase; Provisional
 75-133 1.38e-28

lipoyl synthase; Provisional


Pssm-ID: 235493 [Multi-domain]  Cd Length: 289  Bit Score: 105.55  E-value: 1.38e-28
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515869683  75 RLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGeyataTATIMVG 133
Cdd:PRK05481   6 RKPDWLRVKLPTGEEYTEIKKLLRELGLHTVCEEASCPNIGECWSRG-----TATFMIL 59
PTZ00413 PTZ00413
lipoate synthase; Provisional
 70-132 3.17e-26

lipoate synthase; Provisional


Pssm-ID: 240408 [Multi-domain]  Cd Length: 398  Bit Score: 101.44  E-value: 3.17e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515869683  70 KGERLRLPPWLKTEIPMGKN----YNKLKNTLRNLNLHTVCEEARCPNIGECWGGG-EYATATATIMV 132
Cdd:PTZ00413  87 KRGEEPLPPWFKVKVPKGASrrprFNRIRRSMREKKLHTVCEEAKCPNIGECWGGGdEEGTATATIMV 154
lipA TIGR00510
lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in ...
 65-132 5.84e-22

lipoate synthase; This enzyme is an iron-sulfur protein. It is localized to mitochondria in yeast and Arabidopsis. It generates lipoic acid, a thiol antioxidant that is linked to a specific Lys as prosthetic group for the pyruvate and alpha-ketoglutarate dehydrogenase complexes and the glycine-cleavage system. The family shows strong sequence conservation. [Biosynthesis of cofactors, prosthetic groups, and carriers, Lipoate]


Pssm-ID: 273111  Cd Length: 302  Bit Score: 88.74  E-value: 5.84e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515869683   65 NLKRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGeyataTATIMV 132
Cdd:TIGR00510   6 NPIPNKEILLRKPEWLKIKLPLGTVIAQIKNTMKNKGLHTVCEEASCPNLTECWNHG-----TATFMI 68
PRK12928 PRK12928
lipoyl synthase; Provisional
 72-137 1.30e-21

lipoyl synthase; Provisional


Pssm-ID: 237261  Cd Length: 290  Bit Score: 87.29  E-value: 1.30e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515869683  72 ERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGeyaTATATIMvGPAST 137
Cdd:PRK12928  10 PVERLPEWLRAPIGKASELETVQRLVKQRRLHTICEEARCPNRGECYAQG---TATFLIM-GSICT 71
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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